2LGL
NMR structure of the UHRF1 PHD domain
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 380 |
| Chain | Residue |
| A | CYS315 |
| A | CYS318 |
| A | CYS326 |
| A | CYS329 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 381 |
| Chain | Residue |
| A | CYS331 |
| A | CYS334 |
| A | GLN338 |
| A | HIS354 |
| A | CYS357 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 382 |
| Chain | Residue |
| A | CYS346 |
| A | CYS349 |
| A | CYS373 |
| A | CYS376 |
Functional Information from PROSITE/UniProt
| site_id | PS01359 |
| Number of Residues | 62 |
| Details | ZF_PHD_1 Zinc finger PHD-type signature. CkhCkddvnrlcrvcachlcggrqdpdkq....................LmCde..Cdma.FHiyCldpplssvpsede................................WyCpeC |
| Chain | Residue | Details |
| A | CYS315-CYS376 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 56 |
| Details | Zinc finger: {"description":"PHD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Region: {"description":"Histone H3R2me0 binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Histone H3K4me0 binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Histone H3R2me0 binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"PubMed","id":"15178447","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22837395","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
